(a) The gamma-crystallin which is the major protein by far of young bird and reptile lenses, and which is unique to these classes, exists in situ and after chromatography chiefly in the gamma-helical conformation, in contrast to the lens proteins of all other species examined; (b) the results of our Raman studies on bird (and reptile) lens provide significant evidence that many unusual features of these lenses may depend upon the presence of gamma-crystallin. This protein has very little tryptophan or sulfhydryl, groups which have been implicated in human nuclear cataract formation; (c) Beta-carboline was recently isolated from fluorescent human lens proteins. A very significant development is that we have obtained a high quality pre-resonance Coherent Anti-Stokes Raman spectrum of Beta-caroline (in collaboration with Dr. L.A. Carreira at Univ. of Georgia). This means that the so-called "CARS" technique is fully capable of providing in situ fingerprint information of fluorescent pigments in human lens which are accumulated in the aging process. BIBLIOGRAPHIC REFERENCES: Nai-Teng Yu, Emily J. East, Robert C.C. Chang and J.F.R. Kuck, Jr., "Raman Spectra of Bird and Reptile Lens Proteins", Exp. Eye Res. (1977) 24, 000-000. Nai-Teng Yu, "Raman Spectroscopy: A Conformational Probe in Biochemistry", CRC Critical Rev. in Biochem. (1977), in press.